| pubmed-article:15943588 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15943588 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:15943588 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15943588 | lifeskim:mentions | umls-concept:C1829881 | lld:lifeskim |
| pubmed-article:15943588 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:15943588 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:15943588 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:15943588 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:15943588 | pubmed:dateCreated | 2005-10-10 | lld:pubmed |
| pubmed-article:15943588 | pubmed:abstractText | CBP [CREB (cAMP-response-element-binding protein)-binding protein] and p300 play critical roles in transcriptional co-activation, cell differentiation, proliferation and apoptosis. Multiple transcription factors associate with CBP/p300. With the exception of the SYT oncoprotein, no proteins have been identified that specifically associate with p300, but not CBP. In the present study, we isolated a novel p300-associated protein for which no interaction with CBP was observed by GST (glutathione S-transferase) pull-down assay using Jurkat cell lysates metabolically labelled with [35S]methionine. This protein bound the KIX (kinase-inducible) domain of p300. Following resolution by two-dimensional acrylamide gel electrophoresis, we identified the KIX-domain-bound protein by MS analysis as PRS1 (phosphoribosylpyrophosphate synthetase subunit 1), a protein essential for nucleoside biosynthesis. This is the first report to demonstrate the existence of a p300 KIX-domain-specific-interacting protein that does not interact with CBP. Thus p300 may play a role in the regulation of DNA synthesis through interactions with PRS1. | lld:pubmed |
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| pubmed-article:15943588 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15943588 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15943588 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15943588 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15943588 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15943588 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15943588 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15943588 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:15943588 | pubmed:author | pubmed-author:ShimotohnoKun... | lld:pubmed |
| pubmed-article:15943588 | pubmed:author | pubmed-author:TakaoToshifum... | lld:pubmed |
| pubmed-article:15943588 | pubmed:author | pubmed-author:MatsubaeMasam... | lld:pubmed |
| pubmed-article:15943588 | pubmed:author | pubmed-author:AriumiYasuoY | lld:pubmed |
| pubmed-article:15943588 | pubmed:author | pubmed-author:KaidaAtsushiA | lld:pubmed |
| pubmed-article:15943588 | pubmed:author | pubmed-author:BabaKeikoK | lld:pubmed |
| pubmed-article:15943588 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15943588 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15943588 | pubmed:volume | 391 | lld:pubmed |
| pubmed-article:15943588 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15943588 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15943588 | pubmed:pagination | 239-47 | lld:pubmed |
| pubmed-article:15943588 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15943588 | pubmed:meshHeading | pubmed-meshheading:15943588... | lld:pubmed |
| pubmed-article:15943588 | pubmed:meshHeading | pubmed-meshheading:15943588... | lld:pubmed |
| pubmed-article:15943588 | pubmed:meshHeading | pubmed-meshheading:15943588... | lld:pubmed |
| pubmed-article:15943588 | pubmed:meshHeading | pubmed-meshheading:15943588... | lld:pubmed |
| pubmed-article:15943588 | pubmed:meshHeading | pubmed-meshheading:15943588... | lld:pubmed |
| pubmed-article:15943588 | pubmed:meshHeading | pubmed-meshheading:15943588... | lld:pubmed |
| pubmed-article:15943588 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15943588 | pubmed:articleTitle | Identification of a novel p300-specific-associating protein, PRS1 (phosphoribosylpyrophosphate synthetase subunit 1). | lld:pubmed |
| pubmed-article:15943588 | pubmed:affiliation | Department of Viral Oncology, Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan. | lld:pubmed |
| pubmed-article:15943588 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15943588 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5631 | entrezgene:pubmed | pubmed-article:15943588 | lld:entrezgene |
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